ATP6_ECOLI
ID ATP6_ECOLI Reviewed; 271 AA.
AC P0AB98; P00855; Q2M856; Q47065; Q47708;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; Synonyms=papD, uncB;
GN OrderedLocusNames=b3738, JW3716;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6395859; DOI=10.1042/bj2240799;
RA Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT "DNA sequence around the Escherichia coli unc operon. Completion of the
RT sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT phoS.";
RL Biochem. J. 224:799-815(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6272190; DOI=10.1093/nar/9.16.3919;
RA Gay N.J., Walker J.E.;
RT "The atp operon: nucleotide sequence of the promoter and the genes for the
RT membrane proteins, and the delta subunit of Escherichia coli ATP-
RT synthase.";
RL Nucleic Acids Res. 9:3919-3926(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6278247; DOI=10.1007/bf00271191;
RA Nielsen J., Hansen F.G., Hoppe J., Friedl P., von Meyenburg K.;
RT "The nucleotide sequence of the atp genes coding for the F0 subunits a, b,
RT c and the F1 subunit delta of the membrane bound ATP synthase of
RT Escherichia coli.";
RL Mol. Gen. Genet. 184:33-39(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6277311; DOI=10.1016/0006-291x(81)90495-2;
RA Kanazawa H., Mabuchi K., Kayano T., Noumi T., Sekiya T., Futai M.;
RT "Nucleotide sequence of the genes for F0 components of the proton-
RT translocating ATPase from Escherichia coli: prediction of the primary
RT structure of F0 subunits.";
RL Biochem. Biophys. Res. Commun. 103:613-620(1981).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6301339; DOI=10.1111/j.1749-6632.1982.tb25731.x;
RA Kanazawa H., Futai M.;
RT "Structure and function of H+-ATPase: what we have learned from Escherichia
RT coli H+-ATPase.";
RL Ann. N. Y. Acad. Sci. 402:45-64(1982).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
RX PubMed=2874137; DOI=10.1016/s0021-9258(18)67488-5;
RA Cai B.D., Simoni R.D.;
RT "Impaired proton conductivity resulting from mutations in the a subunit of
RT F1F0 ATPase in Escherichia coli.";
RL J. Biol. Chem. 261:10043-10050(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92.
RX PubMed=6325392; DOI=10.1128/jb.158.1.300-306.1984;
RA Kanazawa H., Kiyasu T., Noumi T., Futai M.;
RT "Overproduction of subunit a of the F0 component of proton-translocating
RT ATPase inhibits growth of Escherichia coli cells.";
RL J. Bacteriol. 158:300-306(1984).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RC STRAIN=K12;
RX PubMed=6318052; DOI=10.1007/bf00327415;
RA Nielsen J., Joergensen B.B., von Meyenburg K., Hansen F.G.;
RT "The promoters of the atp operon of Escherichia coli K12.";
RL Mol. Gen. Genet. 193:64-71(1984).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 235-271.
RX PubMed=2874136; DOI=10.1016/s0021-9258(18)67487-3;
RA Kumamoto C.A., Simoni R.D.;
RT "Genetic evidence for interaction between the a and b subunits of the F0
RT portion of the Escherichia coli proton translocating ATPase.";
RL J. Biol. Chem. 261:10037-10042(1986).
RN [13]
RP MUTAGENESIS.
RX PubMed=2536742; DOI=10.1016/s0021-9258(18)94065-2;
RA Cain B.D., Simoni R.D.;
RT "Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic
RT analysis of the a subunit.";
RL J. Biol. Chem. 264:3292-3300(1989).
RN [14]
RP MUTAGENESIS.
RX PubMed=1829729; DOI=10.1128/jb.173.14.4544-4548.1991;
RA Vik S.B., Lee D., Marshall P.A.;
RT "Temperature-sensitive mutations at the carboxy terminus of the alpha
RT subunit of the Escherichia coli F1F0 ATP synthase.";
RL J. Bacteriol. 173:4544-4548(1991).
RN [15]
RP TOPOLOGY.
RX PubMed=2162353; DOI=10.1016/s0021-9258(18)86981-2;
RA Lewis M.L., Chang J.A., Simoni R.D.;
RT "A topological analysis of subunit alpha from Escherichia coli F1F0-ATP
RT synthase predicts eight transmembrane segments.";
RL J. Biol. Chem. 265:10541-10550(1990).
RN [16]
RP TOPOLOGY.
RX PubMed=2137094; DOI=10.1016/0014-5793(90)80058-q;
RA Bjorbaek C., Foersom V., Michelsen O.;
RT "The transmembrane topology of the a subunit from the ATPase in Escherichia
RT coli analyzed by PhoA protein fusions.";
RL FEBS Lett. 260:31-34(1990).
RN [17]
RP TOPOLOGY.
RX PubMed=8706824; DOI=10.1016/0014-5793(96)00621-7;
RA Yamada H., Moriyama Y., Maeda M., Futai M.;
RT "Transmembrane topology of Escherichia coli H(+)-ATPase (ATP synthase)
RT subunit a.";
RL FEBS Lett. 390:34-38(1996).
RN [18]
RP TOPOLOGY.
RX PubMed=9632683; DOI=10.1074/jbc.273.26.16241;
RA Valiyaveetil F.I., Fillingame R.H.;
RT "Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP
RT synthase.";
RL J. Biol. Chem. 273:16241-16247(1998).
RN [19]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [20]
RP STRUCTURE BY NMR OF 95-271.
RX PubMed=10580496; DOI=10.1038/46224;
RA Rastogi V.K., Girvin M.E.;
RT "Structural changes linked to proton translocation by subunit c of the ATP
RT synthase.";
RL Nature 402:263-268(1999).
CC -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC in the translocation of protons across the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01393, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01393, ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
CC -!- CAUTION: Was originally proposed to be encoded from either Met-1 or
CC Val-71 (PID CAA23521); it is now thought to start of Met-1.
CC {ECO:0000305|PubMed:6278247}.
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DR EMBL; J01594; AAA24731.1; -; Genomic_DNA.
DR EMBL; X01631; CAA25776.1; -; Genomic_DNA.
DR EMBL; V00264; CAA23514.1; -; Genomic_DNA.
DR EMBL; V00266; CAA23520.1; -; Genomic_DNA.
DR EMBL; V00266; CAA23521.1; -; Genomic_DNA.
DR EMBL; V00310; CAA23590.1; -; Genomic_DNA.
DR EMBL; M25464; AAA83869.2; -; Genomic_DNA.
DR EMBL; M14019; AAA24740.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62090.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76761.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77550.1; -; Genomic_DNA.
DR EMBL; X01383; CAA25641.1; -; Genomic_DNA.
DR EMBL; M29174; AAA24423.1; -; Genomic_DNA.
DR PIR; C93732; LWEC6.
DR RefSeq; NP_418194.1; NC_000913.3.
DR RefSeq; WP_000135625.1; NZ_SSZK01000036.1.
DR PDB; 1C17; NMR; -; M=95-271.
DR PDB; 5T4O; EM; 6.90 A; K=1-271.
DR PDB; 5T4P; EM; 7.77 A; K=1-271.
DR PDB; 5T4Q; EM; 8.53 A; K=1-271.
DR PDB; 6OQR; EM; 3.10 A; a=1-271.
DR PDB; 6OQS; EM; 3.30 A; a=1-271.
DR PDB; 6OQT; EM; 3.10 A; a=1-271.
DR PDB; 6OQU; EM; 3.20 A; a=1-271.
DR PDB; 6OQV; EM; 3.30 A; a=1-271.
DR PDB; 6OQW; EM; 3.10 A; a=1-271.
DR PDB; 6PQV; EM; 3.30 A; a=1-271.
DR PDB; 6VWK; EM; 3.30 A; a=1-271.
DR PDB; 6WNQ; EM; 3.40 A; a=1-271.
DR PDB; 6WNR; EM; 3.30 A; a=1-271.
DR PDBsum; 1C17; -.
DR PDBsum; 5T4O; -.
DR PDBsum; 5T4P; -.
DR PDBsum; 5T4Q; -.
DR PDBsum; 6OQR; -.
DR PDBsum; 6OQS; -.
DR PDBsum; 6OQT; -.
DR PDBsum; 6OQU; -.
DR PDBsum; 6OQV; -.
DR PDBsum; 6OQW; -.
DR PDBsum; 6PQV; -.
DR PDBsum; 6VWK; -.
DR PDBsum; 6WNQ; -.
DR PDBsum; 6WNR; -.
DR AlphaFoldDB; P0AB98; -.
DR SMR; P0AB98; -.
DR BioGRID; 4262600; 50.
DR ComplexPortal; CPX-4022; ATP synthase complex.
DR DIP; DIP-47956N; -.
DR IntAct; P0AB98; 2.
DR MINT; P0AB98; -.
DR STRING; 511145.b3738; -.
DR ChEMBL; CHEMBL1075074; -.
DR TCDB; 3.A.2.1.1; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR jPOST; P0AB98; -.
DR PaxDb; P0AB98; -.
DR PRIDE; P0AB98; -.
DR EnsemblBacteria; AAC76761; AAC76761; b3738.
DR EnsemblBacteria; BAE77550; BAE77550; BAE77550.
DR GeneID; 66672358; -.
DR GeneID; 948252; -.
DR KEGG; ecj:JW3716; -.
DR KEGG; eco:b3738; -.
DR PATRIC; fig|1411691.4.peg.2962; -.
DR EchoBASE; EB0097; -.
DR eggNOG; COG0356; Bacteria.
DR HOGENOM; CLU_041018_1_0_6; -.
DR InParanoid; P0AB98; -.
DR OMA; FTHAVRL; -.
DR PhylomeDB; P0AB98; -.
DR BioCyc; EcoCyc:ATPB-MON; -.
DR BioCyc; MetaCyc:ATPB-MON; -.
DR EvolutionaryTrace; P0AB98; -.
DR PRO; PR:P0AB98; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IPI:ComplexPortal.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IMP:EcoCyc.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IMP:EcoCyc.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IMP:EcoCyc.
DR Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR42823; PTHR42823; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..271
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082053"
FT TOPO_DOM 1..39
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 61..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 121..145
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 167..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 241
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 263..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MUTAGEN 206
FT /note="S->L: Reduced activity."
FT MUTAGEN 207
FT /note="L->Y,F: No change in activity."
FT MUTAGEN 210
FT /note="R->K,I,V,E: Completely defective."
FT MUTAGEN 214
FT /note="N->H: Completely defective."
FT MUTAGEN 214
FT /note="N->V: Reduced activity."
FT MUTAGEN 217
FT /note="A->H: Reduced activity."
FT MUTAGEN 217
FT /note="A->R: Completely defective."
FT MUTAGEN 245
FT /note="H->Y: Reduced activity."
FT CONFLICT 71
FT /note="V -> M (in Ref. 2; CAA23521)"
FT /evidence="ECO:0000305"
FT CONFLICT 179..182
FT /note="TLQP -> RCST (in Ref. 4; CAA23590)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="F -> S (in Ref. 6; AAA24740)"
FT /evidence="ECO:0000305"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:6OQU"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6WNR"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 47..64
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 74..93
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 147..180
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 189..228
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 235..268
FT /evidence="ECO:0007829|PDB:6OQR"
SQ SEQUENCE 271 AA; 30303 MW; 4933EAF09401566D CRC64;
MASENMTPQD YIGHHLNNLQ LDLRTFSLVD PQNPPATFWT INIDSMFFSV VLGLLFLVLF
RSVAKKATSG VPGKFQTAIE LVIGFVNGSV KDMYHGKSKL IAPLALTIFV WVFLMNLMDL
LPIDLLPYIA EHVLGLPALR VVPSADVNVT LSMALGVFIL ILFYSIKMKG IGGFTKELTL
QPFNHWAFIP VNLILEGVSL LSKPVSLGLR LFGNMYAGEL IFILIAGLLP WWSQWILNVP
WAIFHILIIT LQAFIFMVLT IVYLSMASEE H
